Proteins Homologous to p47 and p67 Support Superoxide Production by NAD(P)H Oxidase 1 in Colon Epithelial Cells
Open accessAbstract
Superoxide production by phagocytes involves activation of a multi-component NADPH oxidase. Recently, several homologues of the catalytic component of the phagocyte oxidase, gp91phox, were identified in various tissues. Here we describe two proteins, p41 and p51, with significant homology to two cytosolic components of the phagocytic oxidase, p47phox and p67phox. Like p47phox, p41 contains an amino-terminal Phox homology domain, two SH3 domains, and a conserved carboxyl-terminal, proline-rich motif. Similarly, p51 is homologous to p67phox, containing four amino-terminal tetratrico-peptide repeats, a conserved "activation domain" motif, a PB1 domain, and a carboxyl-terminal SH3 domain. The highest levels of p41 transcript are detected in the colon and in other gastrointestinal tissues that express Nox1, the predominant gp91phox homologue in these tissues. In contrast, the p51 transcript showed a more widespread expression pattern, suggesting that it may support other tissue-specific oxidases. Mouse colon in situ hybridization detected both transcripts in the epithelial cells of colon crypts. Heterologous co-expression of p41 and p51 significantly enhances the superoxide-generating activity of Nox1-expressing cells; thus, p41 and p51 appear to be novel regulators of Nox1. These proteins also support the activity of gp91phox, albeit at much lower levels than the cytosolic phox counterparts. Our results suggest colon epithelial cells contain a multi-component NAD(P)H oxidase with a molecular architecture similar to the phagocytic oxidase.
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NOX1 activation requires p22phox, NOX-organizer 1 (NOXO1), NOX-activator 1 (NOXA1), and the GTPase Rac1.
“NOX1 activation requires p22phox, NOX-organizer 1 (NOXO1), NOX-activator 1 (NOXA1), and the GTPase Rac1 (24, 108, 348).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [348]
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- Authors
- Geiszt, M., Lekstrom, K., Witta, J., & Leto, T. L.
- Affiliations
- Semmelweis University (HU)
- National Institutes of Health (US)
- Uniformed Services University of the Health Sciences (US)
- Corresponding author
- Leto, Thomas L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 22
- Pages
- 20006-20012
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2022385815
- Cited by
- 280
- References
- 28
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 3 · 2023: 5 · 2022: 7 · 2021: 2 · 2020: 5 · 2019: 10 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 4 · 2014: 11 · 2013: 10 · 2012: 15
- FWCI
- 10.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- NOX1, p41, p47phox, p67phox, superoxide production, colonic epithelial cells, gp91phox, phox homology domain, SH3 domain, PB1 domain, colonic crypts, gastrointestinal tissue
- MeSH terms
- Amino Acid Sequence, Animals, Colon, DNA-Binding Proteins, Epithelial Cells, Molecular Sequence Data, Phosphoproteins, RNA, Messenger, Superoxides, Transcription Factors, Trans-Activators, Genes, Tumor Suppressor, Sequence Homology, Amino Acid, In Situ Hybridization, NADPH Oxidases, Tumor Suppressor Proteins, Mice
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